OTE_DROME
ID OTE_DROME Reviewed; 424 AA.
AC P20240; Q9V8E5;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Otefin {ECO:0000303|PubMed:2186029};
DE AltName: Full=LEM domain-containing protein Otefin {ECO:0000305};
GN Name=Ote {ECO:0000303|PubMed:2186029, ECO:0000312|FlyBase:FBgn0266420};
GN ORFNames=CG5581 {ECO:0000312|FlyBase:FBgn0266420};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-424, FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=2186029; DOI=10.1016/s0021-9258(19)39001-5;
RA Padan R., Nainudel-Epszteyn S., Goitein R., Fainsod A., Gruenbaum Y.;
RT "Isolation and characterization of the Drosophila nuclear envelope otefin
RT cDNA.";
RL J. Biol. Chem. 265:7808-7813(1990).
RN [5]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DEVELOPMENTAL STAGE.
RX PubMed=2517292; DOI=10.1242/jcs.94.3.463;
RA Harel A., Zlotkin E., Nainudel-Epszteyn S., Feinstein N., Fisher P.A.,
RA Gruenbaum Y.;
RT "Persistence of major nuclear envelope antigens in an envelope-like
RT structure during mitosis in Drosophila melanogaster embryos.";
RL J. Cell Sci. 94:463-470(1989).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=8999964; DOI=10.1074/jbc.272.4.2493;
RA Ashery-Padan R., Weiss A.M., Feinstein N., Gruenbaum Y.;
RT "Distinct regions specify the targeting of otefin to the nucleoplasmic side
RT of the nuclear envelope.";
RL J. Biol. Chem. 272:2493-2499(1997).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION AT SER-54, AND MUTAGENESIS OF SER-54.
RX PubMed=9199347; DOI=10.1128/mcb.17.7.4114;
RA Ashery-Padan R., Ulitzur N., Arbel A., Goldberg M., Weiss A.M., Maus N.,
RA Fisher P.A., Gruenbaum Y.;
RT "Localization and posttranslational modifications of otefin, a protein
RT required for vesicle attachment to chromatin, during Drosophila
RT melanogaster development.";
RL Mol. Cell. Biol. 17:4114-4123(1997).
RN [8]
RP INTERACTION WITH LAM, AND SUBCELLULAR LOCATION.
RX PubMed=9632815; DOI=10.1128/mcb.18.7.4315;
RA Goldberg M., Lu H., Stuurman N., Ashery-Padan R., Weiss A.M., Yu J.,
RA Bhattacharyya D., Fisher P.A., Gruenbaum Y., Wolfner M.F.;
RT "Interactions among Drosophila nuclear envelope proteins lamin, otefin, and
RT YA.";
RL Mol. Cell. Biol. 18:4315-4323(1998).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=16439308; DOI=10.1016/j.ejcb.2005.10.002;
RA Wagner N., Kagermeier B., Loserth S., Krohne G.;
RT "The Drosophila melanogaster LEM-domain protein MAN1.";
RL Eur. J. Cell Biol. 85:91-105(2006).
RN [10]
RP FUNCTION, INTERACTION WITH MED, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18410727; DOI=10.1016/j.devcel.2008.02.018;
RA Jiang X., Xia L., Chen D., Yang Y., Huang H., Yang L., Zhao Q., Shen L.,
RA Wang J., Chen D.;
RT "Otefin, a nuclear membrane protein, determines the fate of germline stem
RT cells in Drosophila via interaction with Smad complexes.";
RL Dev. Cell 14:494-506(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44; SER-50; SER-54; SER-192;
RP SER-198; SER-321; THR-324; SER-326; THR-358; SER-378 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [12]
RP PHOSPHORYLATION AT SER-44; THR-63; SER-152 AND SER-378, FUNCTION,
RP INTERACTION WITH AURA; LAM; ALPHATUB84B; GAMMATUB23C; GAMMATUB37C,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-63.
RX PubMed=22751930; DOI=10.1128/mcb.00814-12;
RA Habermann K., Mirgorodskaya E., Gobom J., Lehmann V., Mueller H.,
RA Bluemlein K., Deery M.J., Czogiel I., Erdmann C., Ralser M.,
RA von Kries J.P., Lange B.M.;
RT "Functional analysis of centrosomal kinase substrates in Drosophila
RT melanogaster reveals a new function of the nuclear envelope component
RT otefin in cell cycle progression.";
RL Mol. Cell. Biol. 32:3554-3569(2012).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23806619; DOI=10.1016/j.devcel.2013.05.023;
RA Barton L.J., Pinto B.S., Wallrath L.L., Geyer P.K.;
RT "The Drosophila nuclear lamina protein otefin is required for germline stem
RT cell survival.";
RL Dev. Cell 25:645-654(2013).
RN [14]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24700158; DOI=10.1534/genetics.114.162941;
RA Barton L.J., Wilmington S.R., Martin M.J., Skopec H.M., Lovander K.E.,
RA Pinto B.S., Geyer P.K.;
RT "Unique and shared functions of nuclear lamina LEM domain proteins in
RT Drosophila.";
RL Genetics 197:653-665(2014).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27174470; DOI=10.1016/j.ydbio.2016.05.001;
RA Barton L.J., Lovander K.E., Pinto B.S., Geyer P.K.;
RT "Drosophila male and female germline stem cell niches require the nuclear
RT lamina protein Otefin.";
RL Dev. Biol. 415:75-86(2016).
CC -!- FUNCTION: Inner nuclear membrane protein (PubMed:2186029,
CC PubMed:9199347, PubMed:18410727, PubMed:22751930). Involved in the
CC attachment of membrane vesicles to chromatin during nuclear assembly,
CC and is probably required for centrosome maturation and cell cycle
CC progression during mitosis (PubMed:9199347, PubMed:22751930). Essential
CC for differentiation of certain tissues and the maintenance of
CC progenitor cell populations (PubMed:18410727, PubMed:24700158,
CC PubMed:23806619, PubMed:27174470). Required for the differentiation and
CC maintenance of male and female germline stem cells (GSCs), as well as
CC the maintenance of somatic cells in the GSC niche (PubMed:18410727,
CC PubMed:23806619, PubMed:27174470). This role is likely to be
CC independent of the BMP (Dpp) pathway that negatively regulates bam
CC transcription during GSC differentiation (PubMed:18410727,
CC PubMed:23806619). During development, plays essential and redundant
CC functions with the other LEM domain proteins; bocks and MAN1
CC (PubMed:24700158). Also has a redundant but important role with bocks
CC during larval development (PubMed:24700158).
CC {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:2186029,
CC ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:23806619,
CC ECO:0000269|PubMed:24700158, ECO:0000269|PubMed:27174470,
CC ECO:0000269|PubMed:9199347}.
CC -!- SUBUNIT: Interacts with Med (PubMed:18410727). Interacts with Lam
CC (PubMed:9632815, PubMed:22751930). Interacts with aurA, alphaTub84B,
CC gammaTub23C and gammaTub37C (PubMed:22751930).
CC {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:22751930,
CC ECO:0000269|PubMed:9632815}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:18410727,
CC ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292,
CC ECO:0000269|PubMed:27174470, ECO:0000269|PubMed:8999964,
CC ECO:0000269|PubMed:9199347, ECO:0000269|PubMed:9632815}; Peripheral
CC membrane protein {ECO:0000269|PubMed:2517292,
CC ECO:0000269|PubMed:8999964, ECO:0000269|PubMed:9199347}; Nucleoplasmic
CC side {ECO:0000269|PubMed:2517292}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:8999964}. Cytoplasm {ECO:0000269|PubMed:22751930,
CC ECO:0000269|PubMed:9199347}. Chromosome {ECO:0000269|PubMed:22751930,
CC ECO:0000269|PubMed:2517292}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:2186029,
CC ECO:0000269|PubMed:22751930}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:22751930}.
CC Note=Component of the spindle envelope during early mitotic cycles
CC (PubMed:2186029, PubMed:2517292). Following nuclear envelope breakdown,
CC becomes dispersed in the cytoplasm and concentrated at the spindle
CC poles (PubMed:22751930, PubMed:2517292). At anaphase (when the nuclear
CC envelope begins to reassemble), locates to the chromosomes accumulating
CC first in areas adjacent to centrosomes and at the peripheral sites of
CC the chromosomes (PubMed:22751930, PubMed:2517292). At telophase,
CC expressed as a continuous rim around the chromatin and increased
CC expression in the midspindle area (PubMed:22751930). During
CC cytokinesis, locates to the nuclear periphery with some remaining in
CC the cytoplasm and at the mid-body (PubMed:22751930). At stage 4 of egg
CC development, expression in the oocyte nuclear envelope is higher than
CC in the nurse nuclear envelope (PubMed:9199347). Expression in oocyte
CC cytoplasm increases after stages 6 to 7 of egg development
CC (PubMed:9199347). {ECO:0000269|PubMed:2186029,
CC ECO:0000269|PubMed:22751930, ECO:0000269|PubMed:2517292,
CC ECO:0000269|PubMed:9199347}.
CC -!- TISSUE SPECIFICITY: Expressed in all cell types of the germarium and
CC testis (PubMed:18410727, PubMed:27174470). Expressed in nurse cells,
CC follicle cells and oocytes (PubMed:9199347).
CC {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:27174470,
CC ECO:0000269|PubMed:9199347}.
CC -!- DEVELOPMENTAL STAGE: Relatively high levels of expression in eggs and
CC 1st instar larvae compared to pupal and adult stages, with weak
CC expression in 2nd instar larvae (at protein level) (PubMed:16439308).
CC Expressed throughout development in all somatic cells (PubMed:9199347).
CC Highest levels of expression in embryos and weak expression in larvae
CC and adults (PubMed:2186029, PubMed:9199347). Expressed throughout
CC development (at protein level) (PubMed:2517292).
CC {ECO:0000269|PubMed:16439308, ECO:0000269|PubMed:2186029,
CC ECO:0000269|PubMed:2517292, ECO:0000269|PubMed:9199347}.
CC -!- PTM: Phosphorylation at Thr-63 by aurA may be required for exit from
CC mitosis (PubMed:22751930). May be phosphorylated by Cdk1 and Pka-C1
CC (PubMed:9199347). {ECO:0000269|PubMed:22751930,
CC ECO:0000269|PubMed:9199347}.
CC -!- DISRUPTION PHENOTYPE: No obvious phenotype (PubMed:18410727,
CC PubMed:23806619, PubMed:24700158). However females are sterile and
CC aging males become prematurely sterile (PubMed:18410727,
CC PubMed:23806619). Males and females exhibit a range of defects in their
CC germarium that may be age dependent phenotypes (PubMed:18410727,
CC PubMed:23806619, PubMed:27174470). Most phenotypes result from defects
CC in germline stem cell (GSC) differentiation that often lead to GSC loss
CC (PubMed:23806619, PubMed:27174470). Also affects somatic cells of the
CC ovarian stem cell niche, with delayed terminal filament formation and
CC cap cell loss (PubMed:27174470). In 10 day old males, stem cell niches
CC display a decrease in hub cell number but somatic cyst stem cells are
CC unaffected (PubMed:27174470). No significant decrease in adult
CC survival, however double mutants with either bocks or Man1 do not
CC survive to the adult stage (PubMed:24700158). Double bocks and Ote
CC mutant larvae have small brains, their imaginal disks are reduced in
CC size or absent, and only 10% of second-instar larvae reach the pupal
CC stage (PubMed:24700158). In Ote and MAN1 double mutants, pupal survival
CC and larval development is unaffected (PubMed:24700158).
CC {ECO:0000269|PubMed:18410727, ECO:0000269|PubMed:23806619,
CC ECO:0000269|PubMed:24700158, ECO:0000269|PubMed:27174470}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35530.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF57722.3; -; Genomic_DNA.
DR EMBL; AY051940; AAK93364.1; -; mRNA.
DR EMBL; X17495; CAA35530.1; ALT_INIT; mRNA.
DR PIR; A35360; A35360.
DR RefSeq; NP_476664.2; NM_057316.5.
DR AlphaFoldDB; P20240; -.
DR SMR; P20240; -.
DR BioGRID; 62771; 27.
DR IntAct; P20240; 11.
DR MINT; P20240; -.
DR STRING; 7227.FBpp0085947; -.
DR iPTMnet; P20240; -.
DR PaxDb; P20240; -.
DR PRIDE; P20240; -.
DR DNASU; 37090; -.
DR EnsemblMetazoa; FBtr0086768; FBpp0085947; FBgn0266420.
DR GeneID; 37090; -.
DR KEGG; dme:Dmel_CG5581; -.
DR UCSC; CG5581-RA; d. melanogaster.
DR CTD; 37090; -.
DR FlyBase; FBgn0266420; Ote.
DR VEuPathDB; VectorBase:FBgn0266420; -.
DR eggNOG; ENOG502TAEI; Eukaryota.
DR GeneTree; ENSGT00530000067345; -.
DR HOGENOM; CLU_652607_0_0_1; -.
DR InParanoid; P20240; -.
DR OMA; TTTYEYK; -.
DR OrthoDB; 1019223at2759; -.
DR PhylomeDB; P20240; -.
DR SignaLink; P20240; -.
DR BioGRID-ORCS; 37090; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 37090; -.
DR PRO; PR:P20240; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0266420; Expressed in egg cell and 23 other tissues.
DR Genevisible; P20240; DM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005641; C:nuclear envelope lumen; IDA:UniProtKB.
DR GO; GO:0005637; C:nuclear inner membrane; IDA:FlyBase.
DR GO; GO:0031965; C:nuclear membrane; IDA:FlyBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0060250; P:germ-line stem-cell niche homeostasis; IMP:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0031468; P:nuclear membrane reassembly; IDA:FlyBase.
DR GO; GO:0048477; P:oogenesis; HMP:FlyBase.
DR GO; GO:0030513; P:positive regulation of BMP signaling pathway; IGI:FlyBase.
DR Gene3D; 1.10.720.40; -; 1.
DR InterPro; IPR011015; LEM/LEM-like_dom_sf.
DR InterPro; IPR003887; LEM_dom.
DR Pfam; PF03020; LEM; 1.
DR SMART; SM00540; LEM; 1.
DR SUPFAM; SSF63451; SSF63451; 1.
DR PROSITE; PS50954; LEM; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton; Membrane;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..424
FT /note="Otefin"
FT /id="PRO_0000206151"
FT DOMAIN 1..30
FT /note="LEM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00313"
FT REGION 1..50
FT /note="Required for binding to Med and germline stem cell
FT maintenance"
FT /evidence="ECO:0000269|PubMed:18410727"
FT REGION 42..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..400
FT /note="Required for binding to Med"
FT /evidence="ECO:0000269|PubMed:18410727"
FT REGION 400..424
FT /note="Essential for nuclear membrane localization and
FT germline stem cell maintenance"
FT /evidence="ECO:0000269|PubMed:18410727"
FT REGION 406..424
FT /note="Essential for nuclear membrane localization"
FT /evidence="ECO:0000269|PubMed:8999964"
FT MOTIF 92..99
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 99..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:22751930"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:9199347"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 63
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22751930"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22751930"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897,
FT ECO:0000269|PubMed:22751930"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MUTAGEN 54
FT /note="S->A: Loss of phosphorylation by Cdk1."
FT /evidence="ECO:0000269|PubMed:9199347"
FT MUTAGEN 63
FT /note="T->A: Prevents phosphorylation and displays an
FT increase in the number of mitotic cells."
FT /evidence="ECO:0000269|PubMed:22751930"
FT MUTAGEN 63
FT /note="T->E: Phosphomimetic mutant which displays a
FT decrease in the number of mitotic cells."
FT /evidence="ECO:0000269|PubMed:22751930"
FT CONFLICT 116
FT /note="I -> V (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="D -> E (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="S -> P (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="P -> S (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="T -> S (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="N -> K (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="A -> S (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="T -> H (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="A -> S (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="L -> V (in Ref. 1; CAA35530)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46584 MW; 51E3A83284F7988B CRC64;
MADVDDFDSL SNAELRAKML AQGLPNIPVT DSSRKVLVKR LRASIGGQAS PAASPKKTNR
RETLAPAPGA PSAPAAASTP VDKLDGNKVA PATKARRTIT AAEAKEPVRR LPEEAIRRRP
DEADRLRSEE PVAARKPTTA PAAQPVQTRR TSTSSGSERK VVEPLRKPET IVEQPASSKR
ADREENYLKV NSLIVLESDE EEDEQLVQAA DLVEQEHAAR QKTTKLASSG TTTYEYKSKV
VEPPRRQVYE ATAAPVLPPS VPSARAQTTS STRSYDYASN PAPGRYSSFV RTAAQGYVTA
EAPPVASYSS SYKRTYANEL SDDTDSKEDQ YESTFARNLA RLRAERIGDR ISPYSRRTLA
SGNAGSGSLG YEPRARRSLR PNDNSVSEAF NRWLNSLEQK YHIKSKLFIV LLVLLLIGVY
YIFY
